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  The tetragonal surface layer of Clostridium aceticum: three-dimensional structure and comparison with the hexagonal layer of Clostridium thermohydrosulfuricum

Woodcock, C. L., Engelhardt, H., & Baumeister, W. (1986). The tetragonal surface layer of Clostridium aceticum: three-dimensional structure and comparison with the hexagonal layer of Clostridium thermohydrosulfuricum. European Journal of Cell Biology., 42(2), 211-217.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-74F4-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-74F5-6
Genre: Journal Article

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 Creators:
Woodcock, C. L., Author
Engelhardt, H.1, Author              
Baumeister, W.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: Bacterial Proteins; *Clostridium/ul [Ultrastructure]; Comparative Study; Computer Simulation; Evolution; Macromolecular Systems; Species Specificity
 Abstract: The regular surface layer (S-layer) of Clostridium aceticum has been isolated and the three-dimensional structure determined to a resolution of 2.0 nm from tilt series of negatively stained preparations. It has tetragonal symmetry with a lattice constant of 12 nm and a thickness of 6 nm; there are probably 4 protein monomers per unit cell. A large proportion of the protein is concentrated in massive "cores" at the major four-fold axes which are situated towards the inner surface of the layer. From these cores, delicate arms extend towards the minor four-fold axes, where secondary connectivity is established near the exterior surface. When viewed from the outside, each of the cores appears to have a large central depression, rather than a true "pore". Since this general pattern of mass distribution is shared by the hexagonal S-layer of Clostridium thermohydrosulfuricum, some consideration has been given to the possible evolutionary steps leading to changes in symmetry. From modelling experiments, it is evident that the change from four-fold to six-fold symmetry in this instance could be accomplished simply by the loss of a structural "domain" from the protomer.

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 Dates: 1986
 Publication Status: Published in print
 Pages: -
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 Rev. Type: -
 Identifiers: eDoc: 318749
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Title: European Journal of Cell Biology.
Source Genre: Journal
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Pages: - Volume / Issue: 42 (2) Sequence Number: - Start / End Page: 211 - 217 Identifier: -